The beta-tubulin monomer release factor (p14) has homology with a region of the DnaJ protein

FEBS Letters
M LlosaJ C Zabala

Abstract

p14 is a molecular chaperone involved in beta-tubulin folding which catalyzes the release of beta-tubulin monomers from intermediate complexes. Here we demonstrate that active p14 protein which we have purified from an overproducing Escherichia coli strain can also release beta-tubulin monomers from tubulin dimers in the presence of an additional cofactor (Z). Analysis of p14 secondary structure suggests that this protein may belong to a family of conserved proteins which share structural similarities with the J-domain of DnaJ. We have constructed deletions and site-directed mutations in the p14 gene. A single D to E mutation in the region shown in DnaJ to be an essential loop for its function affected the monomer-release activity of p14. These results support the hypothesis that this p14 loop interacts with beta-tubulin in a similar fashion as DnaJ interacts with DnaK and suggest a possible role of p14 in the folding process.

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Citations

Jul 13, 1999·Cell Motility and the Cytoskeleton·M L FanarragaJ C Zabala
Jun 11, 2002·Journal of Molecular Biology·Alicia GuaschMiquel Coll
Sep 3, 1999·Molecular Biology of the Cell·P A RadcliffeT Toda
Aug 10, 2010·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Lu LuYi Li
Sep 4, 2012·Cellular and Molecular Life Sciences : CMLS·Gerardo CarranzaJuan Carlos Zabala
Aug 24, 2004·Journal of Molecular Biology·Liru YouTim C Huffaker
Sep 13, 2002·Current Biology : CB·Victor KirikMartin Hülskamp
Oct 3, 2001·Journal of Structural Biology·M Lopez-FanarragaJ C Zabala
Apr 30, 1999·Physiological Reviews·A L Fink
May 11, 2021·Frontiers in Cell and Developmental Biology·Sofia NolascoJuan Carlos Zabala
Apr 21, 2006·Protein Expression and Purification·D KortazarJ C Zabala
Dec 23, 2006·Experimental Cell Research·D KortazarJ C Zabala

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